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  • Leimkühler, S. (2023) Metal-Containing Formate Dehydrogenases, a Personal View, Molecules, 28(4): 5338, doi: 10.3390/molecules28145338
  • Kumar, H., Leimkühler, S. (2023) Changing the Electron Asseptor Specificity of Rhodobacter capsulatus Formate Dehydrogenase from NAD+ to NADP+. Int. J. of Mol. Sci., 24, 16067, doi: 10.3390/ijms242216067
  • Esmaeeli, M., Nimtz, M., Jänsch, L., Ruddock, L.W., Leimkühler, S. (2023) Mechanistic insights into the ROS-mediated inactivation of human aldehyde oxidase. FEBS Letters, 597 (13), p 1792-1801, doi:10.1002/1873-3468.14669
  • Sigurdsson, A., Martins, B.M., Düttmann, S.A., Jasyk, M., Dimos-Röhl, B., Schöpf, F., Gemander, M., Knittel, C.H., Schnegotzki, R., Schmid, B., Kosol, S., Pommerening, L., González-Viegas, M., Seidel, M., Hügelland, M., Leimkühler, S., Dobbek, H., Mainz, A., Süssmuth, R. (2023) Discovery of the lanthipeptide curvocidin and structural insights into its trifunctional synthetase CuvL. Angew. Chem. Int. Ed. Engl. e202302490. doi: 10.1002/anie.202302490
  • Esmaeeli, M., Nimtz, M., Jänsch, L., Ruddock, L.W., Leimkühler, S. (2023) Inactivation of Human Aldehyde Oxidase by Small Sulfhydryl-containing Reducing Agents. Drug. Metab. Dispos. DMD-AR-2022-001244. doi: 10.1124/dmd.122.001244.
  • Haas, R. Engelbrecht, V. Lampret, O., Yadav, S., Apfel, U.P., Leimkühler, S., Happe, T. (2023) The [4Fe-4S]-Cluster of HydF is not Required for the Binding and Transfer of the diiron site of [FeFe]-Hydrogenases. Chembiochem., e202300222 doi: 10.1002/cbic.202300222
  • Kumar, H., Khosraneh, M., Bandaru, S.S.M., Schulzke, C., Leimkühler, S. (2023) The Mechanism of Metal-Containing Formate Dehydrogenases Revisited: The Formation of Bicarbonate as Product Intermediate Provides Evidence for an Oxygen Atom Transfer Mechanism. Molecules., 28(4):1537. doi: 10.3390/molecules28041537
  • Ogunkola, M.O., Guiraude-Capraz, G., Feron, F., Leimkühler, S. (2023) The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells. Biomolecules., 13(1):144. doi: 10.3390/biom13010144


  • Laun, K., Duffus, B.R., Kumar, H., Oudsen, J.P.H., Karafoulidi-Retsou, C., Waffo, A.T., Hildebrandt, P., Ly, K.H., Leimkühler, S., Katz, S., Zegber, I. (2022) A Minimal Light-Driven System to Study the Enzymatic CO2 Reduction of Formate Dehydrogenase. Chem. Cat. Chem. 14(24) doi: 10.1002/cctc.202201067
  • Fujihara, K.M., Zhang, B.Z., Jackson, T.D., Ogunkola, M.O., Nijagal, B., Milne, J.V., Sallmann, D.A., Ang, C.S., Nikolic, I., Kearney, C.J., Hogg, S.J., Cabalag, C.S., Sutton, V.R., Watt, S., Fujihara, A.T. Trapani, J.A., Simpson, K.J., Stojanovski, D., Leimkühler, S., Haupt, S., Phillips, W.A., Clemons, N.J. (2022) Eprenetapopt triggers ferroptosis, inhibits NFS1 cysteine desulfurase, and synergizes with serine and glycine dietary restriction. Sci. Adv., 8(37):eabm9427. doi: 10.1126/sciadv.abm9427.
  • Reeve, H.A., Nicholson, J., Altaf, F., Lonsdale, T.H., Preissler, J., Lauterbach, L., Lenz, O., Leimkühler, S., Hollmann, F., Paul, C.E., Vincent, K.A. (2022) A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H. Chem. Commun. (Camb.), 58(75):10540-10543. doi: 10.1039/d2cc02411j.
  • Stripp, S.T., Duffus, B.R. Fourmond, V., Léger, C., Leimkühler, S., Hirota, S., Hu, Y., Jasniewski, A., Ogata, H., Ribbe, M.W. (2022) Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase. Chem. Rev., 122(14):11900-11973. doi: 10.1021/acs.chemrev.1c00914
  • Laun, K., Duffus, B.R., Wahlefeld, S., Katz, S., Belger, D., Hildebrandt, P., Mroginski, M.A., Leimkühler, S., Zegber, I. (2022) Infrared Spectroscopy Elucidates the Inhibitor Binding Sites in a Metal-Dependent Formate Dehydrogenase. Chemistry. e202201091. doi: 10.1002/chem.202201091.
  • Tiedemann, K., Iobbi-Nivol, C., Leimkühler, S. (2022) The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes. Molecules. 27(9):2993. doi: 10.3390/molecules27092993
  • Takaoka, N., Sanoh, S., Ohta, S., Esmaeeli, M., Leimkühler, S., Kurosaki, M., Terao, M., Garattini, E., Kotake, Y. (2022) Involvement of aldehyde oxidase in the metabolism of aromatic and aliphatic aldehyde-odorants in the mouse olfactory epithelium. Arch. Biochem. Biophys., 715: 109099.doi: 10.1016/


  • Garrido, C., Leimkühler, S. (2021) The Inactivation of Human Aldehyde Oxidase 1 by Hydrogen Peroxide and Superoxide. Drug Metab Dispos, 49(9): 729-735. doi: 10.1124/dmd.121.000549
  • Mota, C. Diniz, A., Coelho, C., Santos-Silva, T., Esmaeeli, M., Leimkühler, S., Cabrita, E.J., Marcelo, F., Romao, M.J. (2021) Interrogating the Inhibition Mechanisms of Human Aldehyde Oxidase by X-ray Crystallography and NMR Spectroscopy: The Raloxifene Case. J. Med. Chem., doi: 10.1021/acs.jmedchem.1c01125
  • Hasnat, A.M., Zupok, A., Olas, J.J., Müller-Röber, B., Leimkühler, S. (2021) A-type carrier proteins are involved in [4Fe-4S] cluster insertion into the radical SAM protein MoaA for the synthesis of active molybdoenzymes. J. Bacteriol.;
  • Yildiz, T., Leimkühler, S. (2021) TusA Is a Versatile Protein That Links Translation Efficiency to Cell Division in Escherichia coli. J. of Bacteriology, 203, 7, e00659-20;
  • Yan, J., Frøkjær, E.E., Engelbrekt, C., Leimkühler., S., Ulstrup, J., Wollenberger, U., Xiao, X., Zhang, J. (2021) Voltammetry and Single-Molecule In Situ Scanning Tunnelling Microscopy of the Redox Metalloenzyme Human Sulfite Oxidase. Chem. Electro. Chem., 8, 164-171;
  • Waffo, A.F.T., Mitrova, B., Tiedemann, K., Iobbi-Nivol, C., Leimkühler, S., Wollenberger, U. (2021) Electrochemical Trimethylamine N-Oxide Biosensor with Enzyme Based Oxygen Scavenging Membrane for Long Term Operation under Ambient Air. Biosensors (MDPI), 11, 98;


  • Mendel, R.R., Hercher, T.W., Zupok, A., Hasnat, M.A., Leimkühler, S. The Requirement of Inorganic Fe-S Clusters for the Biosynthesis of the Organometallic Molybdenum Cofactor. (2020) INORGANICS, 8 (7): doi 10.3390/inorganics8070043
  • Radon, C., Mittelstädt, G., Duffus, B.R., Bürger, J., Hartmann, T., Mielke, T., Teutloff, C., Leimkühler, S., Wendler, P., Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase. (2020) Nat Commun. 11(1):1912 doi: 10.1038/s41467-020-15614-0
  • Leimkühler S., The biosynthesis of the molybdenum cofactors in Escherichia coli. (2020) Environ Microbiol. doi: 10.1111/1462-2920.15003
  • Terao, M., Garattini, E., Romao, M.J., Leimkühler, S., Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes. (2020) J. Biol. Chem. 295(16):5377-5389 doi: 10.1074/jbc.REV119.007741
  • Duffus, B.R., Schrapers, P., Schuth, N., Mebs, S., Dau, H., Leimkühler, S., Haumann, M., Anion Binding and Oxidative Modification at the Molybdenum Cofactor of Formate Dehydrogenase from Rhodobacter capsulatus Studied by X-ray Absorption Spectroscopy. (2020) Inorg Chem. 59(1):214-225 doi: 10.1021/acs.inorgchem.9b01613


  • Tanabe, T.S., Leimkühler, S., Dahl, C., The functional diversity of the prokaryotic sulfur carrier protein TusA. (2019) Adv Microb Physiol. 75:233-277. doi: 101016/bs.ampbs.2019.07.004 
  • Duffus, B.R., Schrapers, P., Schuth, N., Mebs, S., Dau, H., Leimkühler, S., Haumann, M., Anion Binding and Oxidative Modification at the Molybdenum Cofactor of Formate Dehydrogenase from Rhodobacter capsulatus Studied by X-ray Absorption Spectroscopy. (2019) Inorg Chem. doi: 10.1021/acs.inorgchem.9b01613
  • Tang, J., Werchmeister, R.M.L., Preda, L., Huang, W., Zheng, Z.Y., Leimkühler, S., Wollenberger, U., Xiao, X.X., Engelbrekt, C., Ulstrup, J., Zhang, J.D., Three-Dimensional Sulfite Oxidase Bioanodes Based on Graphene Functionalized Carbon Paper for Sulfite/O-2 Biofuel Cells. (2019) ACS CATALYSIS, 9: 6543-6554 
  • Zupok, A., Iobbi-Nivol, C., Méjean, V., Leimkühler, S., The regulation of Moco biosynthesis and molybdoenzyme gene expression by molybdenum and iron in bacteria. (2019) Metallomics; doi: 10.1039/c9mt00186g
  • Lemaire, O.N., Honore, F.A., Tempel, S., Fortier, E. M., Leimkühler, S., Méjean, V., Iobbi-Nivol, C., Shewanella decolorationis LDS1 Chromate Resistance. (2019) Appl. Environ. Microbiol.; 85(18). pii: e00777-19 
  • Zupok, A., Gorka, M., Siemiatkowska, B., Skirycz, A., Leimkühler, S. Iron-Dependent Regulation of Molybdenum Cofactor Biosynthesis Genes in Escherichia coli. (2019) J. Bacteriol.; 201(17). pii: e00382-19
  • Mota C, Esmaeeli M, Coelho C, Santos-Silva T, Wolff M, Foti A, Leimkühler S, Romão MJ. Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (2019) FEBS Open Bio 9:925-934. 
  • Mitrova, B., Waffo, A.F.T., Kaufmann, P., Iobbi-Nivol, C., Leimkühler, S., Wollenberger, U. Electrochemical biosensor for TMAO detection with a chimeric enzyme. (2019) ChemElectroChem.
  • Reschke S, Duffus BR, Schrapers P, Mebs S, Teutloff C, Dau H, Haumann M, Leimkühler S. Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT Cofactor in Escherichia coli. (2019) Biochemistry 58:2228-2242. 
  • Riedel S, Siemiatkowska B, Watanabe M, Müller CS, Schünemann V, Hoefgen R, Leimkühler S. The ABCB7-Like Transporter PexA in Rhodobacter capsulatus Is Involved in the Translocation of Reactive Sulfur Species. (2019) Front Microbiol. 10:406.
  • Neukranz Y, Kotter A, Beilschmidt L, Marelja Z, Helm M, Gräf R, Leimkühler S. Analysis of the Cellular Roles of MOCS3 Identifies a MOCS3-Independent Localization of NFS1 at the Tips of the Centrosome. (2019) Biochemistry 58:1786-1798. 
  • Kaufmann P, Iobbi-Nivol C, Leimkühler S. Reconstitution of Molybdoenzymes with Bis-Molybdopterin Guanine Dinucleotide Cofactors. (2019) Methods Mol Biol. 1876:141-152.
  • Burschel S, Kreuzer Decovic D, Nuber F, Stiller M, Hofmann M, Zupok A, Siemiatkowska B, Gorka M, Leimkühler S, Friedrich T.  Iron-sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I). (2019) Mol Microbiol. 111:31-45.


  • Schanhold, N., Iobbi-Nivol, C., Lehmann, A., Leimkühler, S. Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases. (2018) PLoS One, 13(11):e0201935. doi:101371/journal.pone.0201935. eCollection 2018 
  • Kaufmann, P., Iobbi-Nivol, C., Leimkühler, S. Reconstitution of Molybdoenzymes with Bis-Molybdopterin Guanine Dinucleotide Cofactors. (2018) Methods Mol. Biol., 1876, 141-152, doi: 10.1007/978-1-4939-8864-8_9
  • Burschel, S., Kreuzer Decovic, D., Nuber, F., Stiller, M., Hofmann, M., Zupok, A., Siemiatkowska, B., Gorka, M., Leimkühler, S., Friedrich, T. Iron-Sulfur Cluster Carrier Proteins Involved in the Assembly of Escherichia coli NADH:ubiquinone oxidoreductase (complex I). (2018) Mol. Microbiol., doi: 10.1111/mmi.14137 
  • Lemaire, O.N., Infossi, P., Ali Chaouche, A., Espinosa, L., Leimkühler, S., Giudici-Orticoni, M.T., Mejean, V., Iobbi-Nivol, C. Small membranous proteins of the TorE/NapE family, crutches for cognate respiratory systems in Proteobacteria. (2018) Sci. Rep., 8(1), 13576, doi: 10.1038/s41598-018-31851-2
  • Otto, N., Marelja, Z.,Schoofs, A., Kranenburg, H., Bittern, J., Yildirim, K., Berh, D., Bethke, M., Thomas, S., Rode, S., Risse, B., Jiang, X., Pankratz, M., Leimkühler, S., Klämbt, C. The sulfite oxidase Shopper controls neuronal activity by regulating glutamate homeostasis in Drosophila ensheathing glia. (2018) Nat.Commun., 9(1), 3541, doi: 10.1038/s41467-018-05645-z 
  • Kaufmann, P., Duffus, B.R., Teutloff, C., Leimkühler, S. Functional Studies on Oligotropha carboxidovorans Molybdenum-Copper CO Dehydrogenase Produced in Escherichia coli. (2018) Biochemistry, 57(19), 2889-2901, doi: 10.1021/acs.biochem.8b00128
  • Öner, I.H., Querebillo, C.J., David, C., Gernert, U., Walter, C., Driess, M., Leimkühler, S., Ly, K.H., Weidinger, I.M. High Electromagnetic Field Enhancement of TiO2 Nanotube Electrodes. (2018) Angew. Chem. Int. Ed. Engl., 57(24), 7225-7229, doi: 10.1002/anie.201802597 
  • Marelja, Z., Leimkühler, S., Missirlis, F. Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism. (2018) Front Physiol., doi: 10.3389/fphys.2018.00050
  • Kücükgöze, G., Leimkühler, S. Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities. (2018) PLoS One, 13(1), e0191819, doi: 10.1371/journal.pone.0191819 
  • Kaufmann, P., Duffus, B.R., Mitrova, B., Iobbi-Nivol, C., Teutloff, C., Nimtz, M., Jänsch, L. Wollenberger, U., Leimkühler, S. Modulating the Molybdenum Coordination Sphere of Escherichia coli Trimethylamine N-Oxide Reductase. (2018) Biochemistry, 57 (7), 1130-1143, doi: 10.1021/acs.biochem.7b01108


  • McKenna, S.M., Mines, P., Law, P., Kovacs-Schreiner, K., Birmingham, W.R., Turner, N.J., Leimkühler, S., Carnell, A.J.. The continuous oxidation of HMF to FDCA and the immobilisation and stabilisation of periplasmic aldehyde oxidase (PaoABC). (2017) Green Chemistry, 19, 4660-4665, doi: 10.1039/c7gc01696d 
  • Bühning, M., Friemel, M., Leimkühler, S., Functional Complementation Studies Reveal Different Interaction Partners of Escherichia coli IscS and Human NFS1. (2017) Biochemistry, 56(34):4592-4605. doi: 10.1021/acs.biochem.7b00627
  • Foti, A., Dorendorf, F., Leimkühler, S., A single nucleotide polymorphism causes enhanced radical oxygen species production by human aldehyde oxidase. (2017) PloS One, 12(7):e0182061, doi: 10.1371/journal.pone.0182061 
  • Zeng, T., Leimkühler, S., Wollenberger, U., Fourmond, V., Transient Catalytic Voltammetry of Sulfite Oxidase Reveals Rate Limiting Conformational Changes. (2017) J.Am. Chem. Soc., 139(33):11559-11567. doi: 10.1021/jacs.7b05480.
  • Saengdee, P., Promptmas, C., Zeng, T., Leimkühler, S., Wollenberger, U. Third-generation sulfite biosensor based on sulfite oxidase immobilized on aminopropyltriethoxysilane modified indium tin oxide. (2017) Electroanalysis 29, 110-115, 
  • Brietzke, T., Dietz, T., Kelling, A., Schilde, U., Bois, J., Kelm, H., Reh, M., Schmitz, M.,  Körzdörfer, T., Leimkühler, S., Wollenberger, U., Krüger, H.-J., Holdt, H.-J. The 1,6,7,12-Tetraazaperylene Bridging Ligand as an Electron Reservoir and its Disulfonato Derivative as Redox Mediator in an Enzyme-Electrode Process (2017) Chem.Eur.J., chem.201703639. Inside Cover.
  • Paragas, E.M., Humphreys, S.C., Min, J., Joswig-Jones, C.A., Leimkühler, S., Jones, J.P. ecoAO: A Simple System for the Study of Human Aldehyde Oxidases Role in Drug Metabolism (2017) ACS Omega, 2, 4820-4827, doi: 10.1021/acsomega.7b01054 
  • Dong, C., Yang, J. Reschke, S., Leimkühler, S., Kirk, M.L. Vibrational Probes of Molybdenum Cofactor-Protein Interactions in Xanthine Dehydrogenase. (2017) Inorg. Chem. 56(12): 6830-6837. doi: 10.1021/acs.inorgchem.7b00028
  • Kücükgöze, G., Terao, M., Garattini, E., Leimkühler, S. Direct Comparison of the Enzymatic Characteristics and Superoxide Production of the Four Aldehyde Oxidase enzymes Present in Mouse. (2017) Drug Metab Dispos. 45(8):947-955. doi: 10.1124/dmd.117.075937 
  • Bühning, M., Valleriani, A., Leimkühler, S. The Role of SufS Is Restricted to Fe-S Cluster Biosynthesis in Escherichia coli. (2017) Biochemistry, 56:1987-2000
  • Leimkühler, S. Shared function and moonlighting proteins in molybdenum cofactor biosynthesis. (2017) Bio. Chem., doi:10.1515/hsz-2017-0110. in press 
  • Friemel, M., Marelja, Z., Li, K., Leimkühler, S. The N-Terminus of Iron-Sulfur Cluster Assembly Factor ISD11 Is Crucial for Subcellular Targeting and Interaction with I-Cysteine Desulfurase NFS1. (2017) Biochemistry, 56: 1797-1808
  • Reschke, S., Mebs, S., Sigfridsson-Clauss, K.G.V., Kositzki, R., Leimkühler, S., Haumann, M. Protonation and Sulfido versus Oxo Ligation Changes at the Molybdenum Cofactor in Xanthine Dehydrogenase (XDH) Variants Studied by X-ray Absorption Spectroscopy. (2017). Inorganic Chemistry, doi:10.1021/acs.inorgchem.6b02846 
  • Romao, M.J., Coelho, C., Santos-Silva, T., Foti, A., Terao, M., Garattini, E., Leimkühler, S. Structural basis for the role of mammalian aldehyde oxidases in the metabolism of drugs and xenobiotics. (2017) Curr. Opin. Chem. Biol., 37:39-47. doi:10.1016/j.cbpa.2017.01.005.
  • Leimkühler, S., Bühning, M., Beilschmidt, L. Shared Sulfur Mobilization Routes for tRNA Thiolation and Molybdenum Cofactor Biosynthesis in Prokaryotes and Eukaryotes. (2017) Biomolecules., 7(1). pii:E5. doi:10.3390/biom7010005


  • Correia, M.A., Otrelo-Cardoso, A.R., Schwuchow, V., Sigfridsson Clauss, K.G., Haumann, M., Romao, M.J., Leimkühler, S., Santos-Silva, T. The Escherichia coli Periplasmic Aldehyde Oxidoreductase Is an Exceptional Member, of the Xanthine Oxidase Family of Molybdoenzymes. (2016) ACS Chem Biol., 11(10):2923-2935, doi: 10.1021/acschembio.6b00572 
  • Yan, R., Friemel, M., Aloisi, C., Huynen, M., Taylor, I.A., Leimkühler, S., Pastore, A. The Eukaryotic-Specific ISD11 Is a Complex-Orphan Protein with Ability to Bind the Prokaryotic IscS. (2016) PLoS One, 11(7):e0157895. doi:10.1371/journal.pone.015795
  • Zeng, T., Frasca, S., Rumschöttel, J., Koetz, J., Leimkühler, S., Wollenberger, U. Role of Conductive Nanoparticles in the Direct Unmediated Bioelectrocatalysis of Immobilized Sulfite Oxidase (2016) Electroanalysis, 28, 2303-2310. 
  • Han, X.X., Li, J., Öner, I.H., Zhao, B., Leimkühler, S., Hildebrandt, P., Weidinger, I.M. Nickel electrodes as a cheap and versatile platform for studying structure and function of immobilized redox proteins (2016), Analytica Chimica Acta, 941, 35-40.
  • Hartmann, T., Schrapers, P., Utesch, T., Nimtz, M., Rippers, Y., Dau, H., Mroginski, M.A., Haumann, M., Leimkühler, S. (2016) The Molybdenum Active Site of Formate Dehydrogenase Is Capable of Catalyzing C-H Bond Cleavage and Oxygen Atom Transfer Reactions. Biochemistry, 55(16):2381-9. doi: 10.1021/acs.biochem.6b00002 
  • Cazelles, R., Lalaoui, N., Hartmann, T., Leimkühler, S., Wollenberger, U., Antonietti, M., Cosnier, S. (2016) Ready to use bioinformatics analysis as a tool to predict immbilisation strategies for protein direct electron transfer (DET). Biosens. Bioeletron. 85:90-95. doi: 10.1016/j.bios.2016.04.078
  • Terao, M., Romao, M.J., Leimkühler, S., Bolis, M., Fratelli, M., Coelho, C., Santos-Silva, T., Garattini, E. (2016) Structure and function of mammalian aldehyde oxidases. Arch. Toxicol., 90(4):753-80. doi:10.1007/s00204-016-1683-1 
  • Foti, A., Hartmann, T., Coelho, C., Santos-Silva, T., Romao, M.J., Leimkühler, S. (2016) Optimization of the expression of Human Aldehyde Oxidase for Investigations of Single Nucleotide Polymorphisms. Drug. Metab. Dispos., pii: dmd.115.068395
  • Pinyou, P., Ruff, A., Pöller, S., Alsaoub, S., Leimkühler, S., Wollenberger, U., Schuhmann, W. (2016) Wiring of the aldehyde oxidoreductase PaoABC to electrode surfaces via entrapment in low potential phenothiazine-modified redox polymers. Bioelectrochemistry, 109:24-30. doi:10.1016/j.bioelechem.2015.12.005 
  • Leimkühler, S., Iobbi-Nivol, C. (2016) Bacterial molybdoenzymes: old enzymes for new purposes. FEMS Microbiol. Rev., 40(1):1-18. doi:10.1093/femsre/fuv043


  • Spricigo, R., Leimkühler, S., Gorton, L., Scheller, F.W. and Wollenberger, U. (2015) The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active. Eur. J. Inorg. Chem., 3526-3531. doi:10.1002/ejic.201500034 
  • Herter, S., McKenna, S.M., Frazer, A.R., Leimkühler, S., Carnell, A. and Turner, N.J. (2015) Galactose Oxidase Variants for the Oxidation of Amino Alcohols in Enzyme Cascade Synthesis. ChemCatChem, 7, 2313-2317, doi: 10.1002/cctc.201500218
  • Hartmann, T., Schwanhold, N., Leimkühler, S. (2015) Assembly and catalysis of molybdenum or tungsten-containing formate dehydrogenases from bacteria. Biochimica et Biophysica Acta, 1854, 1090-1100, 
  • Hahn, A., Engelhard, C., Reschke, S., Teutloff, C., Bittl, R., Leimkühler, S. and Risse, R. (2015) Structural Insights into the Incorporation of the Mo Cofactor into Sulfite Oxidase from Site-Directed Spin Labeling. Angew. Chem. Int. Ed., 54, 11865-11869, doi: 10.1002/anie.201504772
  • Zeng, T., Leimkühler, S., Koetz, J. and Wollenberger, U. (2015) Effective Electrochemistry of Human Sulfite Oxidase Immobilized on Quantum-Dots-Modified Indium Tin Oxide Electrode. ACS Appl. Mater. Interfaces, 7, 21487-21494, doi: 10.1021/acsami.5b06665 
  • Coelho, C., Foti, A., Hartmann, T., Santos-Silva, T., Leimkühler, S. and Romao, M.J. (2015) Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase. Nature Chemical Biology, 11, doi: 10.1038/NCHEMBIO.1895
  • Zeng, T., Pankratov, D., Falk, M., Leimkühler, S., Shleev, S. and  Wollenberger, U. (2015) Miniature direct electron transfer based sulphite/oxygen enzymatic fuel cells. Biosensors and Bioelectronics, 66, 39-42, doi:10.1016/j.bios.2014.10.080 
  • Mendel, R.R., Leimkühler, S. (2015) The biosynthesis of the molybdenum cofactors. J.Biol.Inorg.Chem., 20(2):337-47. doi: 10.1007/s00775-014-1173-y
  • Yokoyama, K., Leimkühler, S. (2015) The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria. Biochim.Biophys.Acta, 1853(6):1335-1349. doi:10.1016/j.bbamcr.2014.09.021 
  • Schrapers, P., Hartmann, T., Kositzki, R., Dau, H., Reschke, S., Schulzke, C., Leimkühler, S., Haumann, M. (2015), Sulfido and cysteine ligation changes at the molybdenum cofactor during substrate conversion by formate dehydrogenase (FDH) from Rhodobacter capsulatus. Inorg. Chem. 54(7):3260-71. doi:10.1021/ic502880y
  • Contin, A., Frasca, S., Vivekananthan, J., Leimkühler, S., Wollenberger, U., Plumere, N., Schumann, W. (2015) A pH Responsive Redox Hydrogel for Electrochemical Detection of Redox Silent Biocataltic Processes. Control of Hydrogel Solvation. Electroanalysis, 27(4), 938-944. doi:10.1002/elan.201400621 
  • McKenna, S.M., Leimkühler, S., Herter, S., Turner, N.J., Carnell, A.J. (2015) Enzyme cascade reactions: synthesis of furandicarboxylic acid (FDCA) and carboxylic acids using oxidases in tandem. Green Chem., 17, 3271. doi:10.1039/c5gc00707k


  • Fräsdorf, B., Radon, C., Leimkühler, S. (2014) Characterization and Interaxtion Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans, J. Biol. Chem. pii:jbc.M114.605733 
  • Badalyan, A., Dierich, M., Stiba, K., Schwuchow, V., Leimkühler, S., Wollenberger, U. (2014) Electrical Wiring of the Aldehyde Oxidoreductase PaoABC with a Polymer Containing Osmium Redox Centers: Biosensors for Benzaldehyde and GABA, Biosensors, 4 (4), 403-421, doi:10.3390/bios4040403
  • Leimkühler, S. (2014) Connecting the biosynthesis of the molybdenum cofactor, Fe-S clusters, and tRNA thiolation in humans. in: Iron-Sulfur Clusters in Chemistry and Biology, Ed. by T. Rouault, de Gruyter, pp. 513-555 
  • Hall, J., Reschke, S., Cao, H., Leimkühler, S., Hille, R. (2014) The reductive half-reaction of xanthine dehydrogenase from Rhodobacter capsulatus. The role of Glu 232 in catalysis. J. Biol. Chem. pii: jbc.M114.603456
  • Yokoyama, K., Leimkühler, S. (2014) The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria. Biochim Biophy Acta. Doi: 10.1016/j.bbamcr.2014.09.021 
  • Bechi, B., Herter, S., McKenna, S., Riley, C., Leimkühler, S., Turner, N.J., Carnell, A. J. (2014) Catalytic bio-chemo and bio-bio tandem oxidation reactions for amide and carboxylic acid synthesis.Green Chem. Doi: 10.1039/c4gc01321b
  • Mendel, R.R., Leimkühler, S. (2014) The biosynthesis of the molybdenum cofactors. J. of Biol. Inorg. Chem. (in press) 
  • Leimkühler, S. (2014) The Biosynthesis of the Molybdenum Cofactor in Escherichia coli and Its Connection to FeS Cluster Assembly and the Thiolation of tRNA. Andvances in Biology, vol. 2014, Article ID 808569, 21 pages. doi: 10.1155/2014/808569
  • Dong, C., Yang, J., Leimkühler, S., Kirk, M.L. (2014) Pyranopterin Dithiolene Distortions Relevant to Electron Transfer in Xanthine Oxidase/Dehydrogenase. Inorg. Chem. (in press) 
  • Hahn, A., Reschke, S., Leimkühler, S., Risse, R. (2014) Ketoxime Coupling of p-Acetylphenylalanine at Neutral pH for Site-Directed Spin Labeling of Human Sulfite Oxidase. J. Phys. Chem., 118(25):7077-84. doi: 10.1021/jp503471j
  • Dey, P., Adamovski, M., Friebe, S., Badalyan, A., Mutihac, R-C., Paulus, F., Leimkühler, S., Wollenberger, U. and Haag, R. (2014) Dendritic Polyglycerol-Poly(ethylene glycol)-Based Polymer Networks for Biosensing Application. Applied Materials and Interfaces. 
  • Marelja, Z., Dambowsky, M., Bolis, M., Georgiou, M.L., Garattini, E., Missirlis, F., and Leimkühler, S. (2014) The four aldehyde oxidases of Drosophila melanogaster have different gene expression patterns and enzyme substrate specificities. J. Exp Biol. (in press)
  • Cardoso, A.R.C.O., Schwuchow, V., Rodrigues, D., Cabrita, E.J., Leimkühler, S., Romao, M.J., Santos-Silva, T. (2014) Biochemical, Stabilization and Crystallization Studies on a molecular chaperone (PaoD) involved in the maturation of molybdoenzymes. PLoS One, 9(1):e87295. doi: 10.1371/journal.pone.0087295. 
  • Böhmer, N., Hartmann, T., Leimkühler, S. (2014) The chaperone FdsC for Rhodobacter capsulatus formate dehydrogenase binds the bis-molybdopterin guanine dinucleotide cofactor. FEBS Lett, 588(4):531-7. doi: 10.1016/j.febslet.2013.12.033.
  • Otrelo-Cardoso, A.R., Silva Correia, M.A., Schwuchow, V., Svergun, D.I., Romao, M.J., Leimkühler, S., Santos-Silva, T., (2014) Structural data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and preliminary X-ray crystallography analysis. Int. J. Molecular Sciences, 14, doi:10.3390/ijms140x000x


  • Warelow, T.P., Oke, M., Schoepp-Cothenet, B., Dahl, J.U., Bruselat, N., Sivalingam, G.N., Leimkühler, S., Thalassinos, K., Kappler, U., Naismith, J.H., Santini, J.M. (2013) The Respiratory Arsenite Oxidase: Structure and the Role of Residues Surrounding the Rieske Cluster. PLOS One, Vol. 8, Issue 8, e72535 
  • Mahro, M., Bras, N.F., Cerqueira, N M.F.S.A, Teutloff, Ch., Coelho, C., Romao, M.J., Leimkühler, S. (2013) Identification jof crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity. PLOS One, Vol. 8, Issue 12, e82285
  • Reschke, S., Niks, D., Wilson, H.L., Sigridsson, K.G.V., Haumann, M., Rajagopalan, K.V., Hille, R., and Leimkühler, S. (2013) Effect of exchange of the cysteine molybdenum ligand with selenocysteine on structure and function of the active site in human sulfite oxidase. Biochemistry, 52, 8295-8303 
  • Reschke, S., Sigfridsson, K.G.V., Kaufmann, P., Leidel, N., Horn, S., Gast, K., Schulzke, C., Haumann, M., and Leimkühler, S. (2013) Identification of a Bis-molybdopterin Intermediate in Molybdenum Cofactor Biosynthesis in Escherichia coli. Journal of Biological Chemistry, Vol. 288, 41, 29736-29745
  • Badalyan, A., Yoga, E.G., Schwuchow, V., Pöller, S., Schuhmann, W., Leimkühler, S., Wollenberger, U. (2013) Analysis of the interaction of the molybdenum hydroxylase PaoABC from Escherichia coli with positively and negatively charged metal complexes. Electrochemistry Communications, 37, 5-7 
  • Hartmann, T., and Leimkühler, S. (2013) The oxygen-tolerant and NAD+-dependent formate dehydrogenase from Rhodobacter capsulatus is able to catalyze the reduction of CO2 to formate. FEBS Journal, 280, 6083-6096
  • Frasca, S., Molero Milan, A., Guiet, A., Goebel, C., Perez-Caballero, F., Stiba, K., Leimkühler, S., Fischer, A., Wollenberger, U. (2013) Bioelectrocatalysis at mesoporous antimony doped tin oxide electrodes-Electrochemical characterization and direct enzyme communication. Electrochimica Acta, 110, 172-180 
  • Chern Lim, S., Friemel, M., Marum, J.E., Tucker, E.J., Bruno, D.L., Riley, L.G., Christodoulou, J., Kirk, E.P., Boneh, A., DeGennaro, Ch.M., Springer, M., Mootha, V.K., Rouault, T.A., Leimkühler, S., Thorburn, D.R., Compton, A.G. (2013) Mutations in LYRM4, encoding iron-sulfur cluster biogenesis factor ISD11, cause, deficiency of multiple respiratory chain complexes. Human Molecular Genetics, 1-14, doi:10.1093/hmg/ddt295
  • Badalyan, A., Neumann-Schaal, M., Leimkühler, S., Wollenberger, U. (2013) A Biosensor for Aromatic Aldehydes Komprising the Mediator Dependent PaoABC-Aldehyde Oxidoreductase. Electronanalysis, 25, Nr. 1, 101-108 
  • Sivanesan, A., Ly, K.H., Adamkiewicz, W., Stiba, K., Leimkühler, S., Weidinger, I.M. (2013) Tunable Electric Field Enhancement and Redox Chemistry on TiO2 Island Films via Covalent Attachment to Ag or Au Nanostructures. J. Phys. Chem. 117, 11866-11872,
  • Marelja, Z., Mullick Chowdhury, M., Dosche, C., Hille, C., Baumann, O., Löhmannsröben, G., Leimkühler, S. (2013) The L-Cysteine Desulfurase NFS1 Is Localized in the Cytosol where it Provides the Sulfur for Molybdenum Cofactor Biosynthesis in Humans. PLoS ONE 8(4): e60869. doi:10.1371/journal.pone.0060869 
  • Dahl, J.-U., Radon, Ch., Bühning, M., Nimtz, M., Leichert, L.I., Denis, Y., Jourlin-Castelli, C., Iobbi-Nivol, Ch., Mejean, V., Leimkühler, S. (2013) The Sulfur Carrier Protein TusA Has a Pleiotropic Role in Escherichia coli That Also Affects Molybdenum Cofactor Biosynthesis. J. Biol. Chem., 288 (8), 5426-5442
  • Iobbi-Nivol, C., Leimkühler, S. (2013) Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli. Biochem Biophys Acta, 1827, 1086-1101


  • Coelho, C., Mahro, M., Trincao, J., Carvalho, A.T., Ramos, M.J., Terao, M., Garattini, E., Leimkühler, S., Romao, M.J. (2012) The First Mammalian Aldehyde Oxidase Crystal Structure: Insights Into Substrate specificity. J. Biol. Chem., 287(43):40690-702. doi: 10.1074/jbc.M112.390219 
  • Xia., H., Cao, Y., Dai, X., Marelja, Z., Zhou, D., Mo, R., Al-Mahdawi, S., Pook, M.A., Leimkühler, S., Rouault, T.A., Li, K. (2012) Novel frataxin isoforms may contribute to the pathological mechanism of friedreich ataxia. PloS One, 7 (10):e47847. doi: 10.1371/journal.pone.0047847
  • Rademacher., C., Hoffmann, M.C., Lackmann, J.W., Moser, R., Pfänder, Y., Leimkühler, S., Narberhaus, F., Masepohl, B. (2012)  Tellurite resistance gene trgB confers copper tolerance to Rhodobacter capsulatus. Biometals, 25 (5): 995-1008. doi: 10.1007/s10534-012-9566-2 
  • Kalimuthu, P., Leimkühler, S., Bernhardt, P.V., (2012) Catalytic electrochemistry of xanthine dehydrogenase. J. Phys. Chem. B., 116 (38): 11600-7
  • Sivanesan, A., Kalaivani, G., Fischer, A., Stiba, K., Leimkühler, S., Weidinger, M. (2012) Complementary surface-enhanced resonance Raman spectroscopic biodetection of mixed protein solutions by chitosan- and silica-coated plasmon-tuned silver nanoparticles. Anal. Chem., 84 (13):5759-64. doi: 10.1021/ac301001a
  • Kalimuthu, P., Leimkühler, S., Bernhardt, P.V. (2012) Low-Potential Amperometric Enzyme Biosensor for Xanthine and Hypoxanthine. Analytical Chemistry, 84(23):10359-65. doi: 10.1021/ac3025027
  • Mullick Chowdhury, M., Dosche, C., Löhmannsröben, H.-G., Leimkühler, S. (2012) The dual role of the Molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and Molybdenum cofactor biosynthesis in humans. Journal of Biological Chemistry, 287 (21): 17297-307.
  • Hartmann, T., Terao, M., Garattini, E., Teutloff, C. Alfaro, J.F., Jones, J.P., Leimkühler, S. (2012) The Impact of Single Nucleiotide Plymorphisms on Human Aldehyde Oxidase. Drug Metabolism and Disposition. 40, 5, 856-864 
  • Frasca, S., Rojas, O., Salewski, J., Neumann, B., Stiba, K., Weidinger, I.M., Tiersch, B., Leimkühler, S., Koetz, J., Wollenberger, U. (2012) Human sulfite oxidase electrochemistry on gold nanoparticles modified electrode. Bioelectrochemistry, doi:10.1016/j.bioelechem.2011.11.012
  • Sarauli, D., Xu, C., Dietzel, B., Stiba, K., Leimkühler, S., Schulz, B., Lisdat, F. (2012) Thin films of substituted polyanilines: interactions with biomolecular systems. Soft Matter. doi:10.1039/c2sm07261k 
  • Sarauli, D., Riedel, M., Wettstein, C., Hahn, R., Stiba, K., Wollenberger, U., Leimkühler, S., Schmuki, P., Lisdat, F. (2012) Semimetallic TiO2 nanotubes: new interfaces for bioelectrochemical enzymatic catalysis. Journal of Materials Chemistry. doi: 10.1039/c2jm16427b
  • Kikuchi, H., Fujisaki, H., Furuta, T., Okamoto, K., Leimkühler, S., Nishino, T. (2012) Different inhibitory potency of febuxostat towards mammalian and bacterial xanthine oxidoreductases: insight from molecular dynamics. Scientific Reports, 2:331, doi: 10.1038/srep00331


  • Voss, M., Nimtz, M., Leimkühler, S. (2011) Elucidation of the dual role of Mycobacterial MoeZR in molybdenum cofactor biosynthesis and cysteine biosynthesis. PLoS ONE, 6(11):e28170. doi: 10.1371/journal.pone.0028170 
  • Redelberger, D., Seduk, F., Genest, O., Méjean, V., Leimkühler, S., Iobbi-Nivol C. (2011) The YcdY protein of Escherichia coli, an atypical member of the TorD chaperone family. J Bacteriol. 193(23):6512-6. doi: 10.1128/JB.05927-11
  • Samuel, P.P., Horn, S., Döring, A., Havelius, K.G.V., Reschke, S., Leimkühler, S., Haumann, M., Schulzke, C. (2011) A Crystallographic and Mo K-Edge XAS Study of Molybdenum Oxo Bis-, Mono-, and Non-Dithiolene Complexes - First-Shere Coordination Geometry and Noninnocence of Ligands. Eur J Inorg Chem. DOI10.1002: 4387-4399 
  • Dahl, J-U., Urban, A., Bolte, A., Sriyabhaya, P., Donahue, J.L., Nimtz, M., Larson, T.J., Leimkühler, S. (2011) The Identification of a Novel Protein Involved in Molybdenum Cofactor Biosynthesis in Escherichia coli. J Biol Chem. 286(41):35801-12
  • Mahro, M., Coelho, C., Trincao, J., Rodrigues, D., Terao, M., Garattini, E., Saggu, M., Lendzian, F., Hildebrandt, P., Romao, M.J., Leimkühler, S. (2011) Characterization and crystallization of mouse aldehyde oxidase 3: from mouse liver to Escherichia coli heterologous protein expression. Drug Metab Dispos. 39 (10):1939-45. 
  • Leimkühler, S., Wuebbens, M.M., and Rajagopalan, K.V. (2011) The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria. CCR 255(9-10):1129-1144.
  • Kalimuthu, P., Leimkühler, S., Bernhardt, P.V. (2011) Xanthine dehydrogenase electrocatalysis: autocatalysis and novel activity. J Phys Chem B. 115(11):2655-62. 
  • Havelius, K.G., Reschke, S., Horn, S., Döring, A., Niks, D., Hille, R., Schulzke, C., Leimkühler, S., Haumann, M. (2011) Structure of the Molybdenum Site in YedY, a Sulfite Oxidase Homologue from Escherichia coli. Inorg Chem. 50:741-748.
  • Neumann M, Leimkühler S. (2011) The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria. Biochem Res Int. 2011:850924. 
  • Neumann, M., Seduk, F., Iobbi-Nivol, C., Leimkühler, S. (2011) Molybdopterin dinucleotide biosynthesis in Escherichia coli: Identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides. J Biol Chem. 286:1400-8.


  • Gisin J, Müller A, Pfänder Y, Leimkühler S, Narberhaus F, Masepohl B. (2010) A Rhodobacter capsulatus member of a universal permease family imports molybdate and other oxyanions. J Bacteriol. 192:5943-52. 
  • Sezer M, Spricigo R, Utesch T, Millo D, Leimkühler S, Mroginski MA, Wollenberger U, Hildebrandt P, Weidinger IM. (2010) Redox properties and catalytic activity of surface-bound human sulfite oxidase studied by a combined surface enhanced resonance Raman spectroscopic and electrochemical approach. Phys Chem Chem Phys. 12:7894-903.
  • Zhang W, Urban A, Mihara H, Leimkühler S, Kurihara T, Esaki N. (2010) IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli. J Biol Chem. 285:2302-8. 
  • Spricigo, R., Richter, C., Leimkühler, S., Gorton, L. Scheller, F.W., Wollenberger, U. (2010) Sulfite biosensor based on osmium redox polymer wired sulfite oxidase. Colloids and Surfaces A: Physicochemical and Engineering Aspects 354:  314-319.
  • Fischer, M., Thöny, B., Leimkühler, S. (2010) The biosynthesis of Folate and Pterin and their Enzymology. In "Comprehensive Natural Products Chemistry", Mander, L., Lui, H-W., Eds; Elsevier (Oxford), Volume 7, 599-648.


  • Hänzelmann P, Dahl JU, Kuper J, Urban A, Müller-Theissen U, Leimkühler S, Schindelin H. (2009) Crystal structure of YnjE from Escherichia coli, a sulfurtransferase with three rhodanese domains. Protein Sci. 18: 2480-91. 
  • Neumann M, Mittelstädt G, Seduk F, Iobbi-Nivol C, Leimkühler S. (2009) MocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coli. J Biol Chem. 284:21891-8.
  • Wiethaus J, Müller A, Neumann M, Neumann S, Leimkühler S, Narberhaus F, Masepohl B. (2009) Specific interactions between four molybdenum-binding proteins contribute to Mo-dependent gene regulation in Rhodobacter capsulatus. J Bacteriol. 191:5205-15. 
  • Schumann S, Terao M, Garattini E, Saggu M, Lendzian F, Hildebrandt P, Leimkühler S. (2009) Site directed mutagenesis of amino acid residues at the active site of mouse aldehyde oxidase AOX1. PLoS One. 4:e5348.
  • Neumann M, Mittelstädt G, Iobbi-Nivol C, Saggu M, Lendzian F, Hildebrandt P, Leimkühler S. (2009) A periplasmic aldehyde oxidoreductase represents the first molybdopterin cytosine dinucleotide cofactor containing molybdo-flavoenzyme from Escherichia coli. FEBS J. 276:2762-74. 
  • Dietzel, U., Kuper, J., Doebbler, J.A., Schulte, A., Truglio, J.J., Leimkuhler, S., and Kisker, C. (2009) Mechanism of substrate and inhibitor binding of Rhodobacter capsulatus xanthine dehydrogenase. J. Biol. Chem. 284:8768-76.
  • Spricigo, R., Dronov, R., Lisdat, F., Leimkühler, S. Scheller, F.W., and Wollenberger, U. (2009) Electrocatalytic sulfite biosensor with human sulfite oxidase coimmobilized with cytochrome c in a polyelectrolyte containing multilayer. Anal. Bioanal. Chem. 393: 225-33.


  • Neumann, M. and Leimkühler S. (2008) Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli. FEBS J. 275: 5678-89. 
  • Marelja, Z., Stöcklein, Nimtz, M., and Leimkühler, S. (2008) A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. J. Biol. Chem., 283: 25178-85.
  • Genest, O., Neumann, M., Seduk, F., Stöcklein, W., Méjean, V., Leimkühler, S., and Iobbi-Nivol, C. (2008) Dedicated metallochaperone connects apoenzyme and molybdenum cofactor biosynthesis components. J. Biol. Chem. 283: 21433-40. 
  • Schmitz, J., Mullick Chowdhury, M., Hänzelmann, P., Nimtz, M., Lee, E.-Y., Schindelin, H., and Leimkühler, S. (2008) The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins. Biochemistry 47: 6479-89.
  • Spricigo, R., Dronov, R., Rajagopalan, K.V., Lisdat, F., Leimkühler, S., Scheller, F.W., Wollenberger, U. (2008) Electrocatalytically functional multilayer assembly of sulfite oxidase and cytochrome c. Soft Matter, 4, 972-978. 
  • Schumann, S., Saggu, M., Möller, N., Anker, S.D., Lendzian, F., Hildebrandt, P., and Leimkühler, S. (2008) The Mechanism of Assembly and Cofactor Insertion into Rhodobacter capsulatus Xanthine Dehydrogenase. J. Biol. Chem. 283:16602-11.
  • Dronov, R., Kurth, D.G., Möhwald, H., Spricigo, R., Leimkühler, S., Wollenberger, U., Rajagopalan, K.V., Scheller, F.W., Lisdat, F. (2008) Layer-by-Layer Arrangement by Protein-Protein Interaction of Sulfite Oxidase and Cytochrome c Catalyzing Oxidation of Sulfite. J Am Chem Soc. 130:1122-3. 
  • Wollenberger, U., Spricigo, R., Leimkühler, S., and Schröder, K. (2008) Protein Electrodes with Direct Electrochemical Communication. Adv Biochem Eng Biotechnol. 109: 19-64.


  • Neumann, M., Stöcklein, W., and Leimkühler, S. (2007) Transfer of the molybdenum cofactor synthesized by Rhodobacter capsulatus MoeA to XdhC and MobA. J. Biol. Chem. 282: 28493-500. 
  • Neumann, M., Stöcklein, W., Walburger, A., Magalon, A., and Leimkühler, S. (2007) Identification of a specific Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor bound to XdhC before its insertion into xanthine dehydrogenase. Biochemistry 46: 9586-9595.
  • Krepinsky, K. and Leimkühler, S. (2007) Site-directed mutagenesis of the active-site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3: Major differences in substrate specificity between eukaryotic and bacterial homologues. FEBS J. 274:2778-87. 
  • Pauff, J., Hemann, C.F., Jünemann, N., Leimkühler, S., and Hille, R. (2007) The role of Arginine 310 in Catalysis and Substrate Specificity in Xanthine Dehydrogenase from Rhodobacter capsulatus. J. Biol. Chem. 282: 12785-90.
  • Schmitz, J., Wuebbens, M., Rajagopalan, K.V., and Leimkühler, S. (2007) The role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with an ubiquitin fold. Biochemistry 46: 909-916.


  • Neumann, M., Schulte M., Jünemann, N., Stöcklein, W., and Leimkühler, S. (2006) Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase. J. Biol. Chem. 281: 15701-15708. 
  • Hahnewald, R., Leimkühler, S., Vilaseca, A., Acquaviva-Bourdain, C., Lenz, U., and Reiss, J. (2006) A novel MOCS2 mutation reveals coordinated expression of the small and large subunit of molybdopterin synthase. Mol Genet Metab 89:210-3.
  • Leimkühler, S. (2006) Biosynthesis of the Molybdenum Cofactor and its incorporation into Molybdoenzymes. In “The Periplasm”, (M. Ehrmann ed.), ASM press, pp. 260-275.


  • Matthies A., Nimtz M., and Leimkühler S. (2005) Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry. Biochemistry 44:7912-20. 
  • Leimkühler S., Charcosset M., Latour P., Dorche C., Kleppe S., Scaglia F., Szymczak I., Schupp P., Hahnewald R., and Reiss J. (2005) Ten novel mutations in the molybdenum cofactor genes MOCS1 and MOCS2 and in vitro characterization of a MOCS2 mutation that abolishes the binding ability of molybdopterin synthase. Hum Genet. 117:565-70.
  • Leimkühler, S. (2005) Xanthine Dehydrogenase from Rhodobacter capsulatus: Stucture-Function Studies, Mechanism of Assembly and Cofactor Insertion into the Enzyme. In “Flavins and Flavoproteins 2005” (Nishino, T., Miura, R., Tanokura, M., Fukui, K., eds), pp 391-400. ARchiTect inc. publishers, Tokyo, Japan. 
  • Forlani F., Cereda A., Freuer A., Nimtz M., Leimkühler S., and Pagani S. (2005) The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form. FEBS Lett. 579:6786-90.


  • Matthies, A., Rajagopalan, K.V., Mendel, R.R. and Leimkühler, S. (2004) Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. Proc. Natl. Acad. Sci. USA 101: 5946-5951. 
  • Choi, E.-Y., Stockert, A.L., Leimkühler, S., Hille, R. (2004) Studies on the mechanism of action of xanthine oxidase. J. Inorg. Biochem. 98: 841-848.
  • Leimkühler, S., Stockert A.L., Igarashi, K., Nishino, T., and Hille, R. (2004) The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase. J. Biol. Chem. 279: 40437-40444.


  • Leimkühler, S., Hodson, R., George, G. N., and Rajagopalan, K.V. (2003) Recombinant Rhodobacter capsulatus xanthine dehydrogenase, a useful model system for the characterization of protein variants leading to xanthinuria I in humans. J. Biol. Chem. 278: 20802-20811. 
  • Leimkühler, S., Freuer, A., Santamaria Araujo, J.A., Rajagopalan, K.V., and Mendel, R.R. (2003) Mechanistic studies of human MPT synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. J. Biol. Chem.: 278: 26127-26134.
  • Aguey-Zinsou, K.F., Bernhardt, P.V., and Leimkühler, S. (2003) Protein film voltammetry of Rhodobacter capsulatus xanthine dehydrogenase. J. Am. Chem. Soc. 125: 15352-15358.


  • Truglio, J.J., Theis, K., Leimkühler, S., Rappa, R., Rajagopalan, K.V., and Kisker, C. (2002) Crystal structures of the active and alloxanthine inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure 10: 115-125. 
  • Leimkühler, S., and Rajagopalan, K.V. (2002) Identification of the sulfurtransfer pathway for the generation of the dithiolene moiety of molybdopterin in Escherichia coli. In “ Proceedings of the 12th International Symposium on Pteridines and Folates” (Milstien, S., Kapatos, G., Levine, R.A., and Shane, B. eds.), pp. 253-257, Kluwer Academic Publishers, Dordrecht, The Netherlands.


  • Leimkühler, S., and Rajagopalan, K.V. (2001) In vitro incorporation of nascent molybdenum cofactor into human sulfite oxidase. J. Biol. Chem. 276: 1837-1844. 
  • Leimkühler S., and Rajagopalan K.V. (2001) A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J. Biol. Chem. 276: 22024-22031.
  • Leimkühler S., Wuebbens, M.M., and Rajagopalan K.V. (2001) Characterization of Escherichia coli MoeB and its involvement in the activation of MPT synthase for the biosynthesis of the molybdenum cofactor. J. Biol. Chem. 276: 34695-34701.


  • Solomon P.S., Shaw A.L., Young M.D., Leimkühler S., Hanson G.R., Klipp W., and McEwan A.G. (2000) Molybdate-dependent expression of dimethylsulfoxide reductase in Rhodobacter capsulatus. FEMS Letters 190: 203-208.


  • Leimkühler, S., and Klipp, W. (1999) Role of XDHC in molybdenum cofactor insertion into xanthine dehydrogenase of Rhodobacter capsulatus. J. Bacteriol. 181: 2745-2751. 
  • Leimkühler, S., and Klipp, W. (1999) The molybdenum cofactor biosynthesis protein MobA from Rhodobacter capsulatus is required for the activity of molybdenum enzymes containing MGD, but not for xanthine dehydrogenase harboring the MPT cofactor. FEMS Letters 174: 239-246.
  • Shaw, A., Leimkühler, S., Klipp, W., Hanson, G.R., and McEwan, A.G. (1999) Mutational analysis of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter capsulatus. Microbiology 145: 1409-1420. 
  • Leimkühler, S., Angermüller, S., Schwarz, G., Mendel, R.R., and Klipp, W. (1999) Activity of the molybdopterin-containing xanthine dehydrogenase of Rhodobacter capsulatus can be restored by high molybdenum concentrations in a moeA mutant defective in molybdenum cofactor biosynthesis. J. Bacteriol. 181: 5930-5939.


  • Leimkühler, S., Kern, M., Solomon, P.S., McEwan, A.G., Schwarz, G., Mendel, R.R., and Klipp, W. (1998) Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes. Mol. Microbiol. 27: 853-869.


  • Pau, R.N., Klipp, W., and Leimkühler, S. (1997) Molybdenum transport, processing and gene regulation. In: Winkelmann, G., and Carrano, C.J. (eds.), Transition metals in microbial metabolism, pp. 217-234, Harwood Academic Publishers, Amsterdam.


  • Kutsche, M., Leimkühler, S., Angermüller, S., and Klipp, W. (1996) Promoters controlling expression of the alternative nitrogenase and the molybdenum uptake system in Rhodobacter capsulatus are activated by NtrC, independent of σ54, and repressed by molybdenum. J. Bacteriol. 178: 2010-2017.